Open AccessUracil‐DNA glycosylase activities in hyperthermophilic micro‐organisms
Author(s) -
Koulis Athanasios,
Cowan Don A.,
Pearl Laurence H.,
Savva Renos
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08491.x
Subject(s) - hyperthermophile , pyrococcus furiosus , sulfolobus solfataricus , uracil dna glycosylase , dna glycosylase , thermococcus , biology , sulfolobus , thermotoga maritima , biochemistry , sulfolobus acidocaldarius , archaea , dna repair , dna , escherichia coli , gene
Hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. As in mesophilic organisms, specific activities must exist to restore and protect this template function of DNA. In this study we have demonstrated the presence of thermally stable uracil‐DNA glycosylase activities in seven hyperthermophiles; one bacterial: Thermotoga maritima , and six archaeal: Sulfolobus solfataricus, Sulfolobus shibatae, Sulfolobus acidocaldarius, Thermococcus litoralis, Pyrococcus furiosus and Pyrobaculum islandicum . Uracil‐DNA glycosylase inhibitor protein of the Bacillus subtilis bacteriophage PBS1 shows activity against all of these, suggesting a highly conserved tertiary structure between hyperthermophilic and mesophilic uracil‐DNA glycosylases.